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Cooperativity of the SUMO and Ubiquitin Pathways in Genome Stability

Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
Author to whom correspondence should be addressed.
Academic Editors: Wolf-Dietrich Heyer, Thomas Helleday and Fumio Hanaoka
Biomolecules 2016, 6(1), 14;
Received: 16 January 2016 / Revised: 17 February 2016 / Accepted: 23 February 2016 / Published: 25 February 2016
(This article belongs to the Special Issue DNA Damage Response)
Covalent attachment of ubiquitin (Ub) or SUMO to DNA repair proteins plays critical roles in maintaining genome stability. These structurally related polypeptides can be viewed as distinct road signs, with each being read by specific protein interaction motifs. Therefore, via their interactions with selective readers in the proteome, ubiquitin and SUMO can elicit distinct cellular responses, such as directing DNA lesions into different repair pathways. On the other hand, through the action of the SUMO-targeted ubiquitin ligase (STUbL) family proteins, ubiquitin and SUMO can cooperate in the form of a hybrid signal. These mixed SUMO-ubiquitin chains recruit “effector” proteins such as the AAA+ ATPase Cdc48/p97-Ufd1-Npl4 complex that contain both ubiquitin and SUMO interaction motifs. This review will summarize recent key findings on collaborative and distinct roles that ubiquitin and SUMO play in orchestrating DNA damage responses. View Full-Text
Keywords: Ubiquitin; SUMO; STUbL; DNA damage Ubiquitin; SUMO; STUbL; DNA damage
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Nie, M.; Boddy, M.N. Cooperativity of the SUMO and Ubiquitin Pathways in Genome Stability. Biomolecules 2016, 6, 14.

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